ID   BCAT_MONBE              Reviewed;         390 AA.
AC   A9UZ24;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase;
DE            EC=2.6.1.42;
GN   ORFNames=37018;
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154;
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT   metazoans.";
RL   Nature 451:783-788(2008).
CC   -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC       essential branched chain amino acids leucine, isoleucine, and valine.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC         glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC         L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC         glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; CH991550; EDQ89710.1; -; Genomic_DNA.
DR   RefSeq; XP_001745739.1; XM_001745687.1.
DR   AlphaFoldDB; A9UZ24; -.
DR   SMR; A9UZ24; -.
DR   STRING; 81824.XP_001745739.1; -.
DR   EnsemblProtists; EDQ89710; EDQ89710; MONBRDRAFT_37018.
DR   GeneID; 5890778; -.
DR   KEGG; mbr:MONBRDRAFT_37018; -.
DR   eggNOG; KOG0975; Eukaryota.
DR   InParanoid; A9UZ24; -.
DR   OMA; LTEVFAC; -.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IBA:GO_Central.
DR   GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR   GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009098; P:leucine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR   CDD; cd01557; BCAT_beta_family; 1.
DR   Gene3D; 3.20.10.10; -; 1.
DR   Gene3D; 3.30.470.10; -; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR005786; B_amino_transII.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   InterPro; IPR033939; BCAT_family.
DR   PANTHER; PTHR11825; PTHR11825; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   TIGRFAMs; TIGR01123; ilvE_II; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase;
KW   Branched-chain amino acid biosynthesis; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..390
FT                   /note="Branched-chain-amino-acid aminotransferase"
FT                   /id="PRO_0000340237"
FT   MOD_RES         225
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  43290 MW;  EB28EE7558FF59D4 CRC64;
     MAAALRLTPH MRQAYPVVAA PSVARLSTLD ASKLTIETTT QPRERVEKTK LVFGHTFSDH
     MLKCKWDVNE GWAAPTISPY ANLSLAPSSI VLHYAIECFE GMKAFRGDDD RIRLFRPNLN
     MDRLHRSSVR LALPDFDQDE LLKCITELVI KDKDWIPAGR GYSLYLRPTH IGTAEYLGVG
     KSSSSLLFCI NSPSGAYYST GFKPVSLLAD PAYVRAWPGG VGNTKGGCNY APSIYPQSQA
     QAQGCQQVLW LFGEDHEVTE VGTMNLFMYW KNEQGEDELI TPPLDGTILP GVTRQSIVDM
     ARGWNEFKVS ERKFNMGQVS RALKEGRVYE MFGAGTAATV CPIGQIKYLG EDLNVPLALG
     NSGELTNRIW TDIFDIQYGA VEHEWAPVIA